Crystal structures of a dual coenzyme specific glyceraldehyde-3-phosphate dehydrogenase from the enteric pathogen Campylobacter jejuni

• The crystal structure of the GAPDH from C. jejuni (cjGAPDH) in complex with NAD(P) + was determined at 2.25 Å resolution a space group I4122 . contains typical coenzyme binding domain and catalytic domain. ADP resulted some local conformational changes. C ampylobacter is pathogenic bacteria that causes gastrointestinal disorders thus great importance. Phosphorylating Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) ubiquitous cellular enzyme has well-defined role glycolysis other pathways where it catalyses oxidative phosphorylation glyceraldehyde (2-hydroxy-3-oxopropyl dihydrogen phosphate) to 1,3-Bisphosphoglycerate ((2-Hydroxy-3-phosphonooxy-propanoyloxy)phosphonic acid). genome encodes single (CjGAPDH) which displays dual (NAD/NADP) specificity. NAD-specific GAPDHs are given EC classification 1.2.1.12, whereas NADP-specific classed as 1.2.1.13. GAPDH's specificity class 1.2.1.59. Here we present X-ray this (at Å), comprises superimposed structures NAD- NADP- complexes showing structural adaptation allows specificity, consider context pathogen's metabolism. There no previous reports 1.2.1.59 compare two co-enzymes. Furthermore, also report 2.05 Å) complexed nucleoside respect reported “moonlighting” activities GAPDH.